Greek key jellyroll protein motif design: expression and characterization of a first-generation molecule

A protein designed de novo to fold into the Greek key jellyroll structural motif has been studied. Theoretical analyses have indicated that the designed sequence should adopt the β-strand arrangement of the Greek key jellyroll rather than any other arrangement. A synthetic gene was constructed and t...

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Bibliographic Details
Published in:Protein engineering 1995-01, Vol.8 (1), p.13-20
Main Authors: Smith, D.D.S., Pratt, K.A., Sumner, I.G., Henneke, C.M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anilino Naphthalenesulfonates - metabolism
Base Sequence
Circular Dichroism
Escherichia coli
Gene Expression
Genes, Synthetic
Greek key
Mass Spectrometry
Molecular Sequence Data
Protein Conformation
Protein Denaturation
protein design
Protein Engineering - methods
Protein Folding
Protein Structure, Secondary
Proteins - chemistry
Proteins - genetics
Proteins - isolation & purification
Spectrometry, Fluorescence
Urea - pharmacology
β-sheet
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Description
Summary:A protein designed de novo to fold into the Greek key jellyroll structural motif has been studied. Theoretical analyses have indicated that the designed sequence should adopt the β-strand arrangement of the Greek key jellyroll rather than any other arrangement. A synthetic gene was constructed and the protein expressed in Escherichia coli. Circular dichroism spectroscopy is consistent with the protein folding into the designed conformation and also suggests the presence of tertiary structure. Fluorescence spectroscopy showed the single tryptophan to be partially buried, while denaturation studies showed changes in fluorescence to precede alterations in secondary structure.
ISSN:1741-0126
0269-2139
1741-0134
DOI:10.1093/protein/8.1.13